NADH in the context of Respiratory complex I


NADH in the context of Respiratory complex I

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⭐ Core Definition: NADH

Nicotinamide adenine dinucleotide (NAD) is a coenzyme central to metabolism. Found in all living cells, NAD is called a dinucleotide because it consists of two nucleotides joined through their phosphate groups. One nucleotide contains an adenine nucleobase and the other, nicotinamide. NAD exists in two forms: an oxidized and reduced form, abbreviated as NAD and NADH (H for hydrogen), respectively.

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👉 NADH in the context of Respiratory complex I

Respiratory complex I, EC 7.1.1.2 (also known as NADH:ubiquinone oxidoreductase, Type I NADH dehydrogenase and mitochondrial complex I) is the first large protein complex of the respiratory chains of many organisms from bacteria to humans. It catalyzes the transfer of electrons from NADH to coenzyme Q10 (CoQ10) and translocates protons across the inner mitochondrial membrane in eukaryotes or the plasma membrane of bacteria.

This enzyme is essential for the normal functioning of cells, and mutations in its subunits lead to a wide range of inherited neuromuscular and metabolic disorders. Defects in this enzyme are responsible for the development of several pathological processes such as ischemia/reperfusion damage (stroke and cardiac infarction), Parkinson's disease and others.

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NADH in the context of Oxidative phosphorylation

Oxidative phosphorylation or electron transport-linked phosphorylation or terminal oxidation, is the metabolic pathway in which cells use enzymes to oxidize nutrients, thereby releasing chemical energy in order to produce adenosine triphosphate (ATP). In eukaryotes, this takes place inside mitochondria. Almost all aerobic organisms carry out oxidative phosphorylation. This pathway is so pervasive because it releases more energy than fermentation.

In aerobic respiration, the energy stored in the chemical bonds of glucose is released by the cell in glycolysis and subsequently the citric acid cycle, producing carbon dioxide and the energetic electron donors NADH and FADH₂. Oxidative phosphorylation uses these molecules and O2 to produce ATP, which is used throughout the cell whenever energy is needed. During oxidative phosphorylation, electrons are transferred from the electron donors to a series of electron acceptors in a series of redox reactions ending in oxygen, whose reaction releases half of the total energy.

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NADH in the context of Glycolysis

Glycolysis is the metabolic pathway that converts glucose (C6H12O6) into pyruvate and, in most organisms, occurs in the liquid part of cells (the cytosol). The free energy released in this process is used to form the high-energy molecules adenosine triphosphate (ATP) and reduced nicotinamide adenine dinucleotide (NADH). Glycolysis is a sequence of ten reactions catalyzed by enzymes.

The wide occurrence of glycolysis in other species indicates that it is an ancient metabolic pathway. Indeed, the reactions that make up glycolysis and its parallel pathway, the pentose phosphate pathway, can occur in the oxygen-free conditions of the Archean oceans, also in the absence of enzymes, catalyzed by metal ions, meaning this is a plausible prebiotic pathway for abiogenesis.

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NADH in the context of Glycoconjugate

In molecular biology and biochemistry, glycoconjugates are a subfamily for carbohydrates where saccharides are covalently linked with proteins, peptides, lipids. Glycoconjugates are formed in processes termed glycosylation. Glycoconjugates are involved in cell–cell interactions, including cell–cell recognition; in cell–matrix interactions; and in detoxification processes.

Although the important molecular species DNA, RNA, ATP, cAMP, cGMP, NADH, NADPH, and coenzyme A all contain a carbohydrate part, generally they are not considered as glycoconjugates.

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NADH in the context of Lactate dehydrogenase

Lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells. LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NAD to NADH and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another.

LDH exists in four distinct enzyme classes. This article is specifically about the NAD(P)-dependent L-lactate dehydrogenase. Other LDHs act on D-lactate and/or are dependent on cytochrome c: D-lactate dehydrogenase (cytochrome) and L-lactate dehydrogenase (cytochrome).

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